SitesBLAST
Comparing AZOBR_RS19480 FitnessBrowser__azobra:AZOBR_RS19480 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
Q5SKN9 Long-chain-fatty-acid--CoA ligase; Long-chain fatty acyl-CoA synthetase; LC-FACS; EC 6.2.1.3 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
37% identity, 94% coverage: 26:545/556 of query aligns to 18:535/541 of Q5SKN9
- T184 (= T196) binding Mg(2+)
- G302 (= G311) binding tetradecanoyl-AMP
- Q322 (≠ H331) binding tetradecanoyl-AMP
- G323 (≠ M332) binding tetradecanoyl-AMP
- T327 (= T336) binding tetradecanoyl-AMP
- E328 (= E337) binding Mg(2+)
- D418 (= D428) binding tetradecanoyl-AMP
- K435 (= K445) binding tetradecanoyl-AMP
- K439 (≠ I449) binding tetradecanoyl-AMP
P9WQ37 Long-chain-fatty-acid--CoA ligase FadD13; Fatty acyl-CoA ligase; FACL; FACL13; Fatty acyl-CoA synthetase; ACS; FACS; Very-long-chain fatty-acyl-CoA synthetase; ACSVL; EC 6.2.1.3 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
35% identity, 88% coverage: 52:542/556 of query aligns to 30:495/503 of P9WQ37
- K172 (= K204) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Slight increase of susceptibility to proteolysis.
- R195 (= R227) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
- R197 (≠ E229) mutation to A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-195 and A-244.
- V209 (≠ C241) mutation to D: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced. Slight increase of susceptibility to proteolysis.
- A211 (≠ G243) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.
- T214 (≠ Y246) mutation to W: Shows a marked decrease in the activity with lauric and palmitic acid (C12 and C16 fatty acid) with a simultaneous increase in the activity with caprylic acid (C8 fatty acid).
- R244 (≠ G276) mutation to A: Alteration of the strength of the membrane binding; when associated with A-17; A-195; A-195 and A-197.
- A302 (≠ G334) mutation to G: Slight increase of the fatty acyl-CoA ligase activity. Reduced rate of proteolytic degradation.; mutation to W: Does not show activity with small, medium or long acyl chains.
- W377 (= W423) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding. No significant change in the total expression level, however the cytoplasmic expression is low. Slight increase of susceptibility to proteolysis.
- D382 (= D428) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. No significant change in the total expression level, however the cytoplasmic expression is reduced.
- R397 (= R443) mutation to A: Reduction of binding affinity for fatty acids.
- S404 (= S450) mutation to A: Slight reduction of the fatty acyl-CoA ligase activity. Enhanced affinity towards palmitic acid binding.
- G406 (= G452) mutation to L: No effect on the formation of acyl-adenylate intermediate. However, it shows very poor catalytic efficiency to form acyl-CoA.
- K487 (= K534) mutation to A: Strong reduction of the fatty acyl-CoA ligase activity. Reduction of binding affinity for ATP.
Sites not aligning to the query:
- 9 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-195; A-197 and A-244.
- 17 R→A: Alteration of the strength of the membrane binding; when associated with A-9; A-17; A-197 and A-244.
3r44A Mycobacterium tuberculosis fatty acyl coa synthetase (see paper)
34% identity, 88% coverage: 52:542/556 of query aligns to 33:495/502 of 3r44A
Sites not aligning to the query:
1v26B Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
36% identity, 92% coverage: 26:536/556 of query aligns to 11:502/510 of 1v26B
- active site: T177 (= T196), H197 (≠ N216), H223 (= H240), T320 (= T336), E321 (= E337), K432 (≠ I449), W437 (≠ N454)
- binding adenosine monophosphate: G295 (= G311), S296 (≠ A312), A297 (= A313), G316 (≠ M332), Y317 (= Y333), G318 (= G334), L319 (= L335), T320 (= T336), D411 (= D428), K428 (= K445), K432 (≠ I449), W437 (≠ N454)
- binding magnesium ion: T177 (= T196), E321 (= E337)
1v25A Crystal structure of tt0168 from thermus thermophilus hb8 (see paper)
37% identity, 84% coverage: 26:491/556 of query aligns to 11:464/491 of 1v25A
- active site: T177 (= T196), H197 (≠ N216), H223 (= H240), T320 (= T336), E321 (= E337), K432 (≠ I449), W437 (≠ N454)
- binding phosphoaminophosphonic acid-adenylate ester: H223 (= H240), V224 (≠ C241), G295 (= G311), S296 (≠ A312), A297 (= A313), Y317 (= Y333), G318 (= G334), L319 (= L335), T320 (= T336), D411 (= D428), I423 (≠ V440), K432 (≠ I449), W437 (≠ N454)
- binding magnesium ion: T177 (= T196), E321 (= E337)
8i3iA Acyl-acp synthetase structure bound to amp-pnp in the presence of mgcl2 (see paper)
30% identity, 94% coverage: 19:541/556 of query aligns to 4:518/522 of 8i3iA
- binding phosphoaminophosphonic acid-adenylate ester: T172 (= T196), G174 (= G198), T175 (= T199), T176 (= T200), K180 (= K204), G293 (= G311), A294 (= A312), A295 (= A313), Y315 (= Y333), M317 (≠ L335), S318 (≠ T336), D408 (= D428), R423 (= R443)
P0DX84 3-methylmercaptopropionyl-CoA ligase; MMPA-CoA ligase; EC 6.2.1.44 from Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) (see paper)
33% identity, 87% coverage: 62:546/556 of query aligns to 50:535/539 of P0DX84
- H231 (= H240) mutation to A: Retains 74% of wild-type activity.
- W235 (= W244) mutation to A: Almost completely abolishes the activity.
- G302 (= G308) mutation to P: Almost completely abolishes the activity.
- G303 (= G310) mutation to P: Almost completely abolishes the activity.
- W326 (≠ Y333) mutation to A: Retains 7.7% of wild-type activity.
- P333 (≠ G340) mutation to A: Retains 69% of wild-type activity.
- R432 (= R443) mutation to A: Retains 4.3% of wild-type activity.
- K434 (= K445) mutation to A: Retains 36% of wild-type activity.
- D435 (= D446) mutation to A: Retains 76% of wild-type activity.
- K438 (≠ I449) mutation to A: Retains 5.6% of wild-type activity.
- G440 (= G451) mutation to P: Retains 3.6% of wild-type activity.
- G441 (= G452) mutation to P: Retains 2.7% of wild-type activity.
- E442 (= E453) mutation to A: Retains 27% of wild-type activity.
- W443 (≠ N454) mutation to A: Retains 60% of wild-type activity.
- E474 (= E485) mutation to A: Retains 33% of wild-type activity.
- K523 (= K534) Plays an important role in catalysis; mutation to A: Retains 1.6% of wild-type activity.; mutation to E: Retains 1.4% of wild-type activity.; mutation to R: Retains 57% of wild-type activity.
- K526 (= K537) mutation to A: Retains 48% of wild-type activity.
8i6mA Acyl-acp synthetase structure bound to amp-c18:1 (see paper)
30% identity, 94% coverage: 19:541/556 of query aligns to 2:524/528 of 8i6mA
- binding adenosine monophosphate: G291 (= G311), A293 (= A313), G312 (≠ M332), Y313 (= Y333), G314 (= G334), M315 (≠ L335), S316 (≠ T336), D406 (= D428), R421 (= R443)
- binding magnesium ion: M315 (≠ L335), S316 (≠ T336), E317 (= E337)
8i51A Acyl-acp synthetase structure bound to amp-mc7 (see paper)
30% identity, 94% coverage: 19:541/556 of query aligns to 2:524/528 of 8i51A
- binding adenosine monophosphate: G291 (= G311), A293 (= A313), Y313 (= Y333), M315 (≠ L335), S316 (≠ T336), D406 (= D428), R421 (= R443)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: W225 (= W244), G290 (= G310), G312 (≠ M332), G314 (= G334), M315 (≠ L335), P320 (≠ G340), I321 (≠ P341)
8i8dA Acyl-acp synthetase structure bound to mc7-acp (see paper)
30% identity, 94% coverage: 19:541/556 of query aligns to 4:526/529 of 8i8dA
- binding adenosine monophosphate: G292 (= G310), G293 (= G311), A295 (= A313), G314 (≠ M332), Y315 (= Y333), G316 (= G334), M317 (≠ L335), S318 (≠ T336), D408 (= D428), K429 (≠ I449)
- binding 7-methoxy-7-oxidanylidene-heptanoic acid: H223 (= H240), W227 (= W244), G292 (= G310), G316 (= G334), P322 (≠ G340)
- binding N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide: R93 (= R109), P220 (= P237), H223 (= H240), I269 (≠ V286), G432 (= G452)
8jylA Acyl-acp synthetase structure bound to c10-ams (see paper)
30% identity, 94% coverage: 19:541/556 of query aligns to 2:524/527 of 8jylA
- binding magnesium ion: S316 (≠ T336), E317 (= E337)
- binding [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl N-decanoylsulfamate: W225 (= W244), G290 (= G310), G291 (= G311), A292 (= A312), A293 (= A313), G312 (≠ M332), Y313 (= Y333), G314 (= G334), M315 (≠ L335), S316 (≠ T336), I321 (≠ P341), D406 (= D428), R421 (= R443), K427 (≠ I449), W432 (≠ N454)
8i8eA Acyl-acp synthetase structure bound to c18:1-acp (see paper)
30% identity, 94% coverage: 19:541/556 of query aligns to 4:526/530 of 8i8eA
- binding adenosine monophosphate: G292 (= G310), G293 (= G311), A294 (= A312), A295 (= A313), G314 (≠ M332), Y315 (= Y333), M317 (≠ L335), S318 (≠ T336), D408 (= D428), R423 (= R443)
- binding 4'-phosphopantetheine: R93 (= R109), P220 (= P237), H223 (= H240)
8i49A Acyl-acp synthetase structure bound to atp (see paper)
30% identity, 94% coverage: 19:541/556 of query aligns to 4:526/530 of 8i49A
8i22A Acyl-acp synthetase structure bound to pimelic acid monoethyl ester
30% identity, 94% coverage: 19:541/556 of query aligns to 4:526/530 of 8i22A
6ijbB Structure of 3-methylmercaptopropionate coa ligase mutant k523a in complex with amp and mmpa (see paper)
33% identity, 87% coverage: 62:546/556 of query aligns to 50:535/538 of 6ijbB
- active site: T185 (= T196), H205 (≠ N216), H231 (= H240), S329 (≠ T336), E330 (= E337), K438 (≠ I449), W443 (≠ N454), A523 (≠ K534)
- binding 3-(methylsulfanyl)propanoic acid: W235 (= W244), G303 (= G310), A325 (≠ M332), W326 (≠ Y333), G327 (= G334), M328 (≠ L335)
- binding adenosine monophosphate: G303 (= G310), A304 (≠ G311), A305 (= A312), H324 (= H331), W326 (≠ Y333), G327 (= G334), M328 (≠ L335), S329 (≠ T336), Q359 (= Q366), D417 (= D428)
6ihkB Structure of mmpa coa ligase in complex with adp (see paper)
32% identity, 87% coverage: 62:546/556 of query aligns to 50:532/533 of 6ihkB
- active site: T185 (= T196), H202 (≠ N216), H228 (= H240), S326 (≠ T336), E327 (= E337), K435 (≠ I449), W440 (≠ N454), K520 (= K534)
- binding adenosine-5'-diphosphate: H228 (= H240), G300 (= G310), A301 (≠ G311), A302 (= A312), H321 (= H331), A322 (≠ M332), W323 (≠ Y333), G324 (= G334), M325 (≠ L335), S326 (≠ T336), Q356 (= Q366), D414 (= D428), R429 (= R443), K520 (= K534)
8wevA Crystal structure of feruoyl-coa synthetase complexed with amp from amycolatopsis thermoflava
35% identity, 92% coverage: 30:541/556 of query aligns to 8:484/486 of 8wevA
5gtdA O-succinylbenzoate coa synthetase (mene) from bacillus subtilis in complex with the acyl-adenylate intermediate osb-amp (see paper)
29% identity, 93% coverage: 30:545/556 of query aligns to 6:481/484 of 5gtdA
- active site: T151 (= T196), S171 (≠ N216), H195 (= H240), T288 (= T336), E289 (= E337)
- binding adenosine-5'-monophosphate: G263 (= G310), G264 (= G311), Y285 (= Y333), G286 (= G334), M287 (≠ L335), T288 (= T336), D366 (= D428), V378 (= V440)
- binding magnesium ion: F314 (≠ V371), S315 (≠ A372)
- binding 2-succinylbenzoate: H195 (= H240), S197 (≠ N242), A237 (≠ G282), L260 (≠ V307), G262 (≠ T309), G263 (= G310), G286 (= G334), M287 (≠ L335), S292 (≠ G340), Q293 (≠ P341)
5x8fB Ternary complex structure of a double mutant i454ra456k of o- succinylbenzoate coa synthetase (mene) from bacillus subtilis bound with amp and its product analogue osb-ncoa at 1.76 angstrom (see paper)
29% identity, 93% coverage: 30:545/556 of query aligns to 6:481/485 of 5x8fB
- active site: T151 (= T196), S171 (≠ N216), H195 (= H240), T288 (= T336), E289 (= E337), I387 (= I449), N392 (= N454), K470 (= K534)
- binding magnesium ion: Y23 (≠ H47), E24 (≠ G48), H70 (≠ Y94), N178 (≠ T223), L202 (≠ S247), L214 (≠ C259), T296 (≠ V344), L297 (≠ C345), S298 (≠ A346)
- binding o-succinylbenzoyl-N-coenzyme A: K85 (≠ R109), L191 (= L236), P192 (= P237), H195 (= H240), I196 (≠ C241), S197 (≠ N242), A237 (≠ G282), V238 (≠ A283), L260 (≠ V307), G262 (≠ T309), G286 (= G334), M287 (≠ L335), S292 (≠ G340), Q293 (≠ P341), S388 (= S450), G389 (= G451), G390 (= G452), E391 (= E453), K420 (≠ R482), W421 (= W483), K450 (≠ H515), Y451 (= Y516)
5busA O-succinylbenzoate coenzyme a synthetase (mene) from bacillus subtilis, in complex with amp (see paper)
29% identity, 93% coverage: 30:545/556 of query aligns to 5:478/481 of 5busA
- active site: T150 (= T196), S170 (≠ N216), H194 (= H240), T287 (= T336), E288 (= E337)
- binding adenosine monophosphate: H194 (= H240), G262 (= G310), G263 (= G311), S283 (≠ M332), M286 (≠ L335), T287 (= T336), D365 (= D428), V377 (= V440), R380 (= R443), K467 (= K534)
Query Sequence
>AZOBR_RS19480 FitnessBrowser__azobra:AZOBR_RS19480
MTGPFSRTASIFDRGLAPDPANHVPLSPLSFLKRAAKVYPDKPAIRHGRRTITYAQFHDR
VRRFAGALLRAGVRRGDTVSVLAPNVPALLEAHYAVPLAGAVLNALNTRLDAAAIAFILD
HSETKLLIVDRELSPVAKAALARTERPITLVEIADEQAPDAPSLGAVEYEDFLAAADPAP
WHGPDDEWQAIALNYTSGTTGNPKGVVYHHRGAYLNALGNAFTLNVRPESVFLWTLPMFH
CNGWTYSWAVTAAGGTHVCLRRVEPAAIFDAIAELGVTHLCGAPIVLNMLIHAPAAVRRP
APRRVIVGTGGAAPPSAVLAGMATLGFEVVHMYGLTECYGPATVCAPQDGWEDLDADGLA
LQFARQGVNHVAVEDATVLDRETGRPVPADAQTIGEIALRGNTVMKGYLKNPAATKEALK
DGWFRTGDLGVLHPDGYIEVKDRSKDIIISGGENISSLEVEEALYRHPAVLEAAVVARPD
DRWGESPCAFVTVKPGAERPSESDIIQWCRDRIAHYKVPRTVVFSDLPKTSTGKIQKTVL
RDAARELGERREAKSV
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory